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Magnesium in PDB 1qm4: Methionine Adenosyltransferase Complexed with A L-Methionine Analogue

Enzymatic activity of Methionine Adenosyltransferase Complexed with A L-Methionine Analogue

All present enzymatic activity of Methionine Adenosyltransferase Complexed with A L-Methionine Analogue:
2.5.1.6;

Protein crystallography data

The structure of Methionine Adenosyltransferase Complexed with A L-Methionine Analogue, PDB code: 1qm4 was solved by B.Gonzalez, M.A.Pajares, J.A.Hermoso, J.Sanz-Aparicio, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 10.00 / 2.66
Space group P 41 2 2
Cell size a, b, c (Å), α, β, γ (°) 115.200, 115.200, 159.980, 90.00, 90.00, 90.00
R / Rfree (%) 23 / 29

Other elements in 1qm4:

The structure of Methionine Adenosyltransferase Complexed with A L-Methionine Analogue also contains other interesting chemical elements:

Potassium (K) 3 atoms

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Methionine Adenosyltransferase Complexed with A L-Methionine Analogue (pdb code 1qm4). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Methionine Adenosyltransferase Complexed with A L-Methionine Analogue, PDB code: 1qm4:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in 1qm4

Go back to Magnesium Binding Sites List in 1qm4
Magnesium binding site 1 out of 2 in the Methionine Adenosyltransferase Complexed with A L-Methionine Analogue


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Methionine Adenosyltransferase Complexed with A L-Methionine Analogue within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg404

b:32.6
occ:1.00
OXT A:AMB401 1.9 35.4 1.0
OD2 A:ASP180 2.7 28.6 1.0
C A:AMB401 3.0 43.3 1.0
O A:AMB401 3.4 42.6 1.0
CD A:PRO31 3.6 18.6 1.0
CG A:ASP180 3.6 23.6 1.0
OD1 A:ASP180 3.8 25.9 1.0
O A:GLY255 4.1 49.3 1.0
CG A:PRO31 4.1 16.1 1.0
CB A:AMB401 4.3 43.6 1.0
CA A:AMB401 4.3 43.9 1.0
CD2 A:HIS30 4.3 21.4 1.0
CZ A:PHE251 4.5 33.6 1.0
CA A:GLY258 4.5 51.2 1.0
N A:GLY258 4.5 49.5 1.0
NE2 A:HIS30 4.7 23.0 1.0
CG A:HIS30 4.9 21.7 1.0
CA A:HIS30 5.0 15.6 1.0
N A:PRO31 5.0 16.2 1.0
C A:GLY255 5.0 50.1 1.0

Magnesium binding site 2 out of 2 in 1qm4

Go back to Magnesium Binding Sites List in 1qm4
Magnesium binding site 2 out of 2 in the Methionine Adenosyltransferase Complexed with A L-Methionine Analogue


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Methionine Adenosyltransferase Complexed with A L-Methionine Analogue within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg405

b:51.0
occ:1.00
O2 A:SO4402 2.9 49.8 1.0
OG A:SER248 3.0 44.2 1.0
O3 A:SO4402 3.2 51.2 1.0
S A:SO4402 3.5 54.3 1.0
OD1 B:ASP135 3.6 49.6 1.0
CD1 B:ILE323 4.1 40.0 1.0
CB A:SER248 4.3 39.9 1.0
O4 A:SO4402 4.4 49.3 1.0
O1 A:SO4402 4.6 51.5 1.0
CG B:ASP135 4.8 48.5 1.0
N A:SER248 4.9 38.4 1.0
CB A:PRO247 4.9 31.7 1.0

Reference:

B.Gonzalez, M.A.Pajares, J.A.Hermoso, L.Alvarez, F.Garrido, J.R.Sufrin, J.Sanz-Aparicio. The Crystal Structure of Tetrameric Methionine Adenosyltransferase From Rat Liver Reveals the Methionine-Binding Site J.Mol.Biol. V. 300 363 2000.
ISSN: ISSN 0022-2836
PubMed: 10873471
DOI: 10.1006/JMBI.2000.3858
Page generated: Tue Aug 13 11:53:36 2024

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